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Bone morphogenetic protein-1: the type I procollagen C-proteinase
E Kessler1, K Takahara, L Biniaminov
1Maurice and Gabriela Goldschleger Eye Research Institute, Tel Aviv University Sackler Faculty of Medicine, Sheba Medical Center, Tel Hashomer, Israel.
Science (New York, N.Y.)
|January 19, 1996
Summary
Bone morphogenetic protein-1 (BMP-1) is identified as identical to procollagen C-proteinase (PCP). This finding links BMP-1
Area of Science:
- Biochemistry
- Developmental Biology
- Molecular Biology
Background:
- Bone morphogenetic proteins (BMPs) are crucial for bone formation.
- BMP-1, distinct from TGF-beta, is a protease family prototype involved in developmental pattern formation.
- The enzymatic substrates for BMP-1/Tolloid (TLD) family proteins remain largely unknown.
Purpose of the Study:
- To identify the enzymatic activity and substrates of BMP-1.
- To determine the relationship between BMP-1 and procollagen C-proteinase (PCP).
Main Methods:
- Biochemical assays to characterize BMP-1 enzymatic activity.
- Comparison of BMP-1 and PCP protein sequences and functions.
Main Results:
- Bone morphogenetic protein-1 (BMP-1) and procollagen C-proteinase (PCP) are demonstrated to be the same enzyme.
- This enzyme cleaves the COOH-propeptides of procollagens I, II, and III.
Conclusions:
- The identification of BMP-1 as PCP links matrix deposition enzymes to developmental pattern formation genes.
- This discovery provides enzymatic insight into the function of BMP-1/TLD family proteins in development.